4BEB
MUTANT (K220E) OF THE HSDR SUBUNIT OF THE ECOR124I RESTRICTION ENZYME IN COMPLEX WITH ATP
Replaces: 2Y3TFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003677 | molecular_function | DNA binding |
| A | 0004518 | molecular_function | nuclease activity |
| A | 0004519 | molecular_function | endonuclease activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006304 | biological_process | DNA modification |
| A | 0009035 | molecular_function | type I site-specific deoxyribonuclease activity |
| A | 0009307 | biological_process | DNA restriction-modification system |
| A | 0016787 | molecular_function | hydrolase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003677 | molecular_function | DNA binding |
| B | 0004518 | molecular_function | nuclease activity |
| B | 0004519 | molecular_function | endonuclease activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006304 | biological_process | DNA modification |
| B | 0009035 | molecular_function | type I site-specific deoxyribonuclease activity |
| B | 0009307 | biological_process | DNA restriction-modification system |
| B | 0016787 | molecular_function | hydrolase activity |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003677 | molecular_function | DNA binding |
| C | 0004518 | molecular_function | nuclease activity |
| C | 0004519 | molecular_function | endonuclease activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006304 | biological_process | DNA modification |
| C | 0009035 | molecular_function | type I site-specific deoxyribonuclease activity |
| C | 0009307 | biological_process | DNA restriction-modification system |
| C | 0016787 | molecular_function | hydrolase activity |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003677 | molecular_function | DNA binding |
| D | 0004518 | molecular_function | nuclease activity |
| D | 0004519 | molecular_function | endonuclease activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006304 | biological_process | DNA modification |
| D | 0009035 | molecular_function | type I site-specific deoxyribonuclease activity |
| D | 0009307 | biological_process | DNA restriction-modification system |
| D | 0016787 | molecular_function | hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 1885 |
| Chain | Residue |
| A | THR314 |
| A | ASP408 |
| A | ATP1886 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ATP A 1886 |
| Chain | Residue |
| A | THR309 |
| A | GLY310 |
| A | SER311 |
| A | GLY312 |
| A | LYS313 |
| A | THR314 |
| A | LEU315 |
| A | THR661 |
| A | GLY662 |
| A | ASP664 |
| A | ARG688 |
| A | ARG691 |
| A | MG1885 |
| A | MET227 |
| A | LEU270 |
| A | VAL271 |
| A | MET272 |
| A | ARG273 |
| A | GLN276 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 1885 |
| Chain | Residue |
| B | THR314 |
| B | ASP408 |
| B | ATP1886 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ATP B 1886 |
| Chain | Residue |
| B | LEU270 |
| B | VAL271 |
| B | MET272 |
| B | ARG273 |
| B | GLN276 |
| B | THR309 |
| B | GLY310 |
| B | SER311 |
| B | GLY312 |
| B | LYS313 |
| B | THR314 |
| B | LEU315 |
| B | THR661 |
| B | GLY662 |
| B | ASP664 |
| B | ARG688 |
| B | ARG691 |
| B | MG1885 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG C 1885 |
| Chain | Residue |
| C | THR314 |
| C | ASP408 |
| C | ATP1886 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ATP C 1886 |
| Chain | Residue |
| C | MET227 |
| C | LEU270 |
| C | VAL271 |
| C | MET272 |
| C | ARG273 |
| C | GLN276 |
| C | THR309 |
| C | GLY310 |
| C | SER311 |
| C | GLY312 |
| C | LYS313 |
| C | THR314 |
| C | LEU315 |
| C | THR661 |
| C | GLY662 |
| C | ASP664 |
| C | ARG688 |
| C | ARG691 |
| C | MG1885 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG D 1885 |
| Chain | Residue |
| D | THR314 |
| D | ASP408 |
| D | GLU409 |
| D | ATP1886 |
| site_id | AC8 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ATP D 1886 |
| Chain | Residue |
| D | MET227 |
| D | LEU270 |
| D | VAL271 |
| D | MET272 |
| D | ARG273 |
| D | GLN276 |
| D | THR309 |
| D | GLY310 |
| D | SER311 |
| D | GLY312 |
| D | LYS313 |
| D | THR314 |
| D | THR661 |
| D | GLY662 |
| D | ASP664 |
| D | ARG688 |
| D | ARG691 |
| D | MG1885 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 580 |
| Details | Domain: {"description":"Helicase ATP-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 876 |
| Details | Region: {"description":"Motor 1 domain","evidences":[{"source":"PubMed","id":"32483229","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 48 |
| Details | Region: {"description":"Motor 2-helicase linker","evidences":[{"source":"PubMed","id":"32483229","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Motif: {"description":"DEAH box","evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 128 |
| Details | Region: {"description":"Helicase domain","evidences":[{"source":"PubMed","id":"32483229","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
